Table 1.
High‐density lipoprotein (HDL) composition and anti‐oxidant activity in ApoE mutant mice
| HDL characteristic | B10.RIII.WT | B10.RIII.ApoE +/– | B10.RIII.ApoE –/– |
|---|---|---|---|
| Esterified cholesterol (%) | 18·0 ± 3·5 | 15·4 ± 3·1 | 9·8 ± 3·4*† |
| Free cholesterol (%) | 2·6 ± 0·8 | 3·2 ± 0·8 | 6·5 ± 1·3*† |
| Phospholipids (%) | 27·9 ± 6·2 | 31·1 ± 4·8 | 29·6 ± 5·8 |
| Triglycerides (%) | 8·1 ± 3·8 | 5·3 ± 1·8 | 7·5 ± 1·5 |
| Protein (%) | 43·3 ± 0·4 | 45·0 ± 1·3* | 46·6 ± 2·3* |
| PON1 activity (µmol/ml.min) | 59·3 ± 1·7 | 58·8 ± 4·5 | 45·9 ± 4·9*† |
| LDL oxidation protection (%) | 175·2 ± 8·8 | 185·1 ± 49·3 | 167·9 ± 12·1 |
HDL was isolated from plasma by sequential ultracentrifugation at 100 000 g for 24 h at a density of 1·063–1·21 g/ml, and lipids and protein were determined. Values are expressed as relative (%) chemical composition and correspond to HDL preparations isolated from four pooled samples of four to six mice in each group. Serum plasma arylesterase activity was measured using phenylacetate as substrate and ethylenediamine tetraacetic acid (EDTA)‐sensitive plasma arylesterase (PON1) activity was calculated by subtracting the EDTA‐resistant arylesterase (five animals/group). Human low‐density lipoprotein (LDL) was incubated with 2·5 µM CuSO4 in the presence or absence of purified HDLs (0·1 mM phospholipids) from each mouse strain (three purified pools of HDL/group). The percentage of protection of LDL oxidation is expressed as the mean ± standard deviation (s.d.). Values are mean ± s.d. *P < 0·05 versus B10.RIII.WT mice. † P < 0·05 versus B10.RIII.ApoE +/– mice. ApoE = apolipoprotein E.